The X-Ray Crystal Structures of Primary Aryl Substituted Selenoamides 英文参考文献.docVIP

Molecules 2009, 14, 884-892; doi:10.3390/moleculeOPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Article The X-Ray Crystal Structures of Primary Aryl Substituted Selenoamides Yang Li, Guo-Xiong Hua, Alexandra M. Z. Slawin and J. Derek Woollins * School of Chemistry, University of St Andrews, St Andrews, Fife, Scotland, KY16 9ST, UK * Author to whom correspondence should be addressed; Email: jdw3@st-andrews.ac.uk. Received: 18 December 2009; in revised form: 13 February 2009 / Accepted: 19 February 2009 / Published: 23 February 2009 Abstract: The X-ray structures of 12 primary selenoamides are reported. Metric parameters are provided, together with an illustration of the range of hydrogen bonding motifs. Keywords: Woollins reagent; Primary selenoamides; X-ray structures. Introduction Selenium is an essential element for life; e.g, selenocysteine is recognised as the 21st amino acid and the importance of selenium containing enzymes in redox processes has is now recognized [1-3]. Many organoselenium compounds have been studied as biological models that simulate catalytic functions demonstrated by natural enzymes [4-14]. For example, ebselen (I, Figure 1) acts as a glutathione peroxidase (GPx) mimic and as a scavenger of peroxinitrite and the activity of the sulfur analogue of ebselen was 15-fold lower than that of ebselen [5,6]. Selenazofurin (II) has been reported to be a potent inhibitor of phlebovirus infections [10]. Selenophenfurin (III) exhibits antiproliferative and inosine 5’-monophosphate dehydrogenase (IMPDH)-inhibition activity. Leukotrienes such as leukotriene B4 (LTB4) are important mediators of asthma, allergy, arthritis, psoriasis, and inflammatory bowel disease [11,12]. Galet et al. showed that benzoselenazolinones of type IV and the corresponding diselenides V dramatically decrease the formation of LTB4 [13]. Phe